BRENDA - Enzyme Database show
show all sequences of 1.5.5.2

The structure of the proline utilization a proline dehydrogenase domain inactivated by N-propargylglycine provides insight into conformational changes induced by substrate binding and flavin reduction

Srivastava, D.; Zhu, W.; Johnson, W.H.; Whitman, C.P.; Becker, D.F.; Tanner, J.J.; Biochemistry 49, 560-569 (2010)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Escherichia coli
Crystallization (Commentary)
Crystallization
Organism
2.15 A resolution structure of the PRODH inactivated by N-propargylglycine. The initial events involved in broadcasting the reduced flavin state to the distal membrane-binding domain include major reorganization of the flavin ribityl chain, severe butterfly bending of the isoalloxazine ring, and disruption of an electrostatic network involving the flavin N(5) atom, Arg431, and Asp370. The active site is incompletely assembled in the absence of the substrate, and the binding of proline draws together conserved residues in helix 8 and the beta1-alphal loop to complete the active site
Escherichia coli
Inhibitors
Inhibitors
Commentary
Organism
Structure
N-propargylglycine
irreversibly inactivates PutA by covalently linking the flavin N(5) atom to the epsilon-amino of Lys329. Inactivation locks PutA into a conformation that may mimic the proline-reduced, membrane-associated form
Escherichia coli
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
P09546
-
-
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Escherichia coli
Crystallization (Commentary) (protein specific)
Crystallization
Organism
2.15 A resolution structure of the PRODH inactivated by N-propargylglycine. The initial events involved in broadcasting the reduced flavin state to the distal membrane-binding domain include major reorganization of the flavin ribityl chain, severe butterfly bending of the isoalloxazine ring, and disruption of an electrostatic network involving the flavin N(5) atom, Arg431, and Asp370. The active site is incompletely assembled in the absence of the substrate, and the binding of proline draws together conserved residues in helix 8 and the beta1-alphal loop to complete the active site
Escherichia coli
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
N-propargylglycine
irreversibly inactivates PutA by covalently linking the flavin N(5) atom to the epsilon-amino of Lys329. Inactivation locks PutA into a conformation that may mimic the proline-reduced, membrane-associated form
Escherichia coli
Other publictions for EC 1.5.5.2
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
743834
Huijbers
Proline dehydrogenase from Th ...
Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Sci. Rep.
7
43880
2017
-
-
1
1
1
-
-
3
-
-
-
2
-
6
-
-
-
-
-
-
4
-
4
1
1
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3
1
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3
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1
3
1
1
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4
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4
1
1
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3
1
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-
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3
3
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Homo sapiens, Mus musculus
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2016
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-
2
-
1
-
12
-
2
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4
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1
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12
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2
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2
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6
6
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741858
Cabassa-Hourton
Proteomic and functional anal ...
Arabidopsis thaliana
Biochem. J.
473
2623-2634
2016
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1
1
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741642
Wang
Molecular cloning and express ...
Jatropha curcas
Appl. Biochem. Biotechnol.
175
2413-2426
2015
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1
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6
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-
2
-
-
-
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1
1
2
2
1
-
-
742162
Huijbers
High yields of active Thermus ...
Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Biotechnol. J.
10
395-403
2015
-
1
1
-
-
-
1
-
1
-
3
2
-
5
-
-
1
-
-
-
1
-
6
1
1
-
2
-
1
-
-
1
-
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-
1
1
1
-
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-
-
1
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1
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3
2
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1
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1
-
6
1
1
-
2
-
1
-
-
-
-
1
1
-
-
-
740734
Moxley
Evidence for hysteretic substr ...
Escherichia coli
J. Biol. Chem.
289
3639-3651
2014
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3
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2
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2
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1
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3
3
742487
Schertl
Biochemical characterization ...
Arabidopsis thaliana
FEBS J.
281
2794-2804
2014
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2
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2
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1
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4
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1
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1
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1
2
2
1
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724389
Serrano
Kinetic and isotopic character ...
Mycobacterium tuberculosis
Biochemistry
52
5009-5015
2013
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2
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3
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1
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2
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1
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1
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1
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1
1
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2
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2
2
741732
Kawakami
Comparative analysis of the c ...
Pyrococcus furiosus, Pyrococcus horikoshii, Pyrococcus horikoshii OT-3, Thermococcus kodakarensis, Thermococcus kodakarensis KOD1 JCM12380, Thermococcus profundus, Thermococcus profundus DSM 9503
Appl. Microbiol. Biotechnol.
97
3419-3427
2013
-
-
4
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-
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8
-
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-
13
-
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4
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22
7
4
-
4
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4
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4
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7
7
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-
14
-
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7
-
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-
22
7
7
-
7
-
7
-
-
-
-
8
14
-
-
-
742641
Omidinia
Expression, purification and ...
Pseudomonas putida, Pseudomonas putida POS-F84
Indian J. Microbiol.
53
297-302
2013
-
-
1
-
1
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-
-
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5
-
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1
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2
2
1
1
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1
1
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1
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1
1
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1
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1
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2
2
1
1
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1
1
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1
1
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-
743635
Paes
Proline dehydrogenase regulat ...
Trypanosoma cruzi, Trypanosoma cruzi CL Brener
PLoS ONE
8
e69419
2013
-
-
1
-
-
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-
1
1
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-
2
-
5
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1
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1
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10
1
1
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1
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2
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1
2
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1
1
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2
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1
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1
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10
1
1
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1
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1
2
2
1
-
-
724345
Moxley
Rapid reaction kinetics of pro ...
Escherichia coli
Biochemistry
51
511-520
2012
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1
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2
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739932
Kawakami
L-proline dehydrogenases in hy ...
Pyrococcus horikoshii
Appl. Microbiol. Biotechnol.
93
83-93
2012
-
-
-
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-
1
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3
1
-
5
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1
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1
1
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1
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4
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4
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1
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1
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1
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1
1
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1
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711252
Srivastava
The structure of the proline u ...
Escherichia coli
Biochemistry
49
560-569
2010
-
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1
1
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1
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696361
Ostrander
A conserved active site tyrosi ...
Escherichia coli
Biochemistry
48
951-959
2009
-
-
1
1
2
-
1
6
-
-
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-
-
3
-
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1
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2
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6
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1
3
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1
1
1
2
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6
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1
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2
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671977
Zhu
Exploring the proline-dependen ...
Escherichia coli
Biochemistry
44
12297-12306
2005
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4
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4
1
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2
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1
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1
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4
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4
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4
1
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1
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4
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658033
Zhang
Structures of the Escherichia ...
Escherichia coli
Biochemistry
43
12539-12548
2004
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1
1
1
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3
2
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1
1
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3
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1
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1
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1
2
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3
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1
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1
1
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3
3
2
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1
1
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1
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1
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1
2
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658211
Baban
Probing a hydrogen bond pair a ...
Escherichia coli
Biochim. Biophys. Acta
1701
49-59
2004
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1
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3
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4
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2
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1
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4
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658668
Kawakami
Gene and primary structures of ...
Thermococcus profundus
Extremophiles
8
99-108
2004
-
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1
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1
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1
5
-
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10
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1
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1
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2
1
1
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659987
Lee
Structure of the proline dehyd ...
Escherichia coli
Nat. Struct. Biol.
10
109-114
2003
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392565
Nadaraia
Crystallization and preliminar ...
Escherichia coli
Acta Crystallogr. Sect. D
57
1925-1927
2001
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392570
Sakuraba
Purification, characterization ...
Thermococcus profundus
Appl. Environ. Microbiol.
67
1470-1475
2001
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1
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6
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1
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1
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392572
Chaudhary
-
Proline dehydrogenase activity ...
Vigna radiata
Indian J. Exp. Biol.
37
1234-1240
1999
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-
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1
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392571
Brown
Conformational change and memb ...
Escherichia coli
J. Biol. Chem.
268
8972-8979
1993
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392569
Deutch
-
Oxidation of L-thiazolidine-4- ...
Escherichia coli
J. Gen. Microbiol.
138
1593-1598
1992
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Redesigned purification yields ...
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392555
Wood
Membrane association of prolin ...
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Graham
Proline dehydrogenase from Esc ...
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392560
Scarpulla
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